OTCA_CAMJE
ID OTCA_CAMJE Reviewed; 306 AA.
AC Q9PNU6; Q0P9Q8;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ornithine carbamoyltransferase, anabolic {ECO:0000303|PubMed:22949186};
DE Short=OTCase {ECO:0000303|PubMed:22949186};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109}; OrderedLocusNames=Cj0994c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=22949186; DOI=10.1107/s1744309112031259;
RA Shabalin I.G., Porebski P.J., Cooper D.R., Grabowski M., Onopriyenko O.,
RA Grimshaw S., Savchenko A., Chruszcz M., Minor W.;
RT "Structure of anabolic ornithine carbamoyltransferase from Campylobacter
RT jejuni at 2.7 A resolution.";
RL Acta Crystallogr. F 68:1018-1024(2012).
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline, which is a substrate for argininosuccinate
CC synthetase (ArgG) involved in the final step in arginine biosynthesis.
CC {ECO:0000305|PubMed:22949186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3.
CC {ECO:0000305|PubMed:22949186}.
CC -!- SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000305|PubMed:22949186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR EMBL; AL111168; CAL35112.1; -; Genomic_DNA.
DR PIR; G81374; G81374.
DR RefSeq; WP_002858026.1; NC_002163.1.
DR RefSeq; YP_002344389.1; NC_002163.1.
DR PDB; 3TPF; X-ray; 2.70 A; A/B/C/D/E/F=1-306.
DR PDBsum; 3TPF; -.
DR AlphaFoldDB; Q9PNU6; -.
DR SMR; Q9PNU6; -.
DR IntAct; Q9PNU6; 68.
DR STRING; 192222.Cj0994c; -.
DR PaxDb; Q9PNU6; -.
DR PRIDE; Q9PNU6; -.
DR EnsemblBacteria; CAL35112; CAL35112; Cj0994c.
DR GeneID; 905285; -.
DR KEGG; cje:Cj0994c; -.
DR PATRIC; fig|192222.6.peg.976; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_2_7; -.
DR OMA; DGNNVCN; -.
DR BRENDA; 2.1.3.3; 1087.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_01109; OTCase; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR InterPro; IPR002292; Orn/put_carbamltrans.
DR InterPro; IPR024904; OTCase_ArgI.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..306
FT /note="Ornithine carbamoyltransferase, anabolic"
FT /id="PRO_0000112904"
FT BINDING 46..49
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 73
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 97
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 124..127
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 156
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 220
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 224..225
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 260..261
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 288
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 12..27
FT /evidence="ECO:0007829|PDB:3TPF"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:3TPF"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3TPF"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 227..230
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:3TPF"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3TPF"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:3TPF"
FT HELIX 278..301
FT /evidence="ECO:0007829|PDB:3TPF"
SQ SEQUENCE 306 AA; 34976 MW; 58CBF72AF8C86116 CRC64;
MKHFLTLRDF SKEEILSLVN HASELKKEPK KLLQDKTLAM IFEKNSTRTR MAFELAITEL
GGKALFLSSN DLQLSRGEPV KDTARVIGAM VDFVMMRVNK HETLLEFARY SKAPVINALS
ELYHPTQVLG DLFTIKEWNK MQNGIAKVAF IGDSNNMCNS WLITAAILGF EISIAMPKNY
KISPEIWEFA MKQALISGAK ISLGYDKFEA LKDKDVVITD TWVSMGEENE KERKIKEFEG
FMIDEKAMSV ANKDAILLHC LPAYRGYEVS EEIFEKHADV IFEEARNRLY VVKALLCFLD
NQRGRE
